Header list of 2cq0.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSCRIPTION 19-MAY-05 2CQ0
TITLE SOLUTION STRUCTURE OF RNA BINDING DOMAIN IN EUKARYOTIC TRANSLATION
TITLE 2 INITIATION FACTOR 3 SUBUNIT 4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF;
COMPND 5 SYNONYM: EIF-3 DELTA, EIF3 P44, EIF-3 RNA-BINDING SUBUNIT, EIF3 P42,
COMPND 6 EIF3G;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: EIF3S4;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040510-15;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHEIS
KEYWDS RRM DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 2 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.TSUDA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CQ0 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CQ0 1 VERSN
REVDAT 1 19-NOV-05 2CQ0 0
JRNL AUTH K.TSUDA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF RNA BINDING DOMAIN IN EUKARYOTIC
JRNL TITL 2 TRANSLATION INITIATION FACTOR 3 SUBUNIT 4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CQ0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024491.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.15MM 13C/15N-PROTEIN, 20MM D
REMARK 210 -TRIS-HCL (PH 7.0), 100MM NACL,
REMARK 210 1MM D-DTT, 0.02% NAN3, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9297, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINTED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION, STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 PRO A 231 101.44 -45.76
REMARK 500 1 ASN A 232 97.67 -57.59
REMARK 500 1 ASP A 237 -45.24 -134.03
REMARK 500 1 ASN A 238 152.26 -48.11
REMARK 500 1 ASN A 245 52.07 70.45
REMARK 500 1 PRO A 261 -17.23 -48.02
REMARK 500 1 ILE A 297 -33.72 -37.97
REMARK 500 1 SER A 318 45.23 -93.21
REMARK 500 2 PRO A 261 -17.14 -48.00
REMARK 500 2 LYS A 280 -73.77 -46.87
REMARK 500 2 ILE A 297 -35.16 -39.94
REMARK 500 2 SER A 301 104.47 -59.81
REMARK 500 3 SER A 229 112.76 -35.75
REMARK 500 3 ASN A 232 42.93 -100.52
REMARK 500 3 ALA A 235 106.82 -161.97
REMARK 500 3 ASP A 237 -71.33 -121.31
REMARK 500 3 ASN A 245 38.41 70.79
REMARK 500 3 PRO A 261 -17.21 -48.01
REMARK 500 3 LYS A 280 -75.00 -68.77
REMARK 500 3 ILE A 297 -33.20 -35.04
REMARK 500 3 LYS A 316 150.35 -41.61
REMARK 500 3 PRO A 317 44.59 -77.07
REMARK 500 3 SER A 318 108.18 -44.49
REMARK 500 4 PRO A 261 -17.24 -47.96
REMARK 500 4 ILE A 297 -34.65 -39.86
REMARK 500 4 HIS A 307 27.25 45.91
REMARK 500 4 PRO A 317 156.74 -47.01
REMARK 500 5 ASN A 232 -61.85 -92.56
REMARK 500 5 ASN A 245 38.43 73.58
REMARK 500 5 PRO A 261 -18.29 -47.98
REMARK 500 5 LYS A 280 -72.90 -63.58
REMARK 500 5 ALA A 296 -70.51 -64.50
REMARK 500 5 ILE A 297 -34.72 -35.08
REMARK 500 5 HIS A 307 29.98 47.62
REMARK 500 5 SER A 318 -53.38 -129.17
REMARK 500 5 SER A 321 127.35 -39.90
REMARK 500 6 ASN A 238 159.84 -39.85
REMARK 500 6 ASN A 245 39.06 73.32
REMARK 500 6 PRO A 261 -17.23 -47.93
REMARK 500 6 ASP A 273 -178.61 -68.49
REMARK 500 6 ILE A 297 -35.95 -35.88
REMARK 500 7 PRO A 231 166.99 -45.51
REMARK 500 7 ASP A 237 38.79 35.19
REMARK 500 7 ASN A 245 43.77 71.59
REMARK 500 7 PRO A 261 -17.93 -47.97
REMARK 500 7 THR A 275 -72.38 -55.14
REMARK 500 7 ILE A 297 -32.97 -34.48
REMARK 500 8 SER A 228 171.26 -46.97
REMARK 500 8 ARG A 234 -62.21 -127.69
REMARK 500 8 ALA A 235 -38.84 -35.40
REMARK 500
REMARK 500 THIS ENTRY HAS 133 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001003366 RELATED DB: TARGETDB
DBREF 2CQ0 A 231 320 UNP O75821 IF34_HUMAN 231 320
SEQADV 2CQ0 GLY A 224 UNP O75821 CLONING ARTIFACT
SEQADV 2CQ0 SER A 225 UNP O75821 CLONING ARTIFACT
SEQADV 2CQ0 SER A 226 UNP O75821 CLONING ARTIFACT
SEQADV 2CQ0 GLY A 227 UNP O75821 CLONING ARTIFACT
SEQADV 2CQ0 SER A 228 UNP O75821 CLONING ARTIFACT
SEQADV 2CQ0 SER A 229 UNP O75821 CLONING ARTIFACT
SEQADV 2CQ0 GLY A 230 UNP O75821 CLONING ARTIFACT
SEQADV 2CQ0 SER A 321 UNP O75821 CLONING ARTIFACT
SEQADV 2CQ0 GLY A 322 UNP O75821 CLONING ARTIFACT
SEQADV 2CQ0 PRO A 323 UNP O75821 CLONING ARTIFACT
SEQADV 2CQ0 SER A 324 UNP O75821 CLONING ARTIFACT
SEQADV 2CQ0 SER A 325 UNP O75821 CLONING ARTIFACT
SEQADV 2CQ0 GLY A 326 UNP O75821 CLONING ARTIFACT
SEQRES 1 A 103 GLY SER SER GLY SER SER GLY PRO ASN ARG ARG ALA ASP
SEQRES 2 A 103 ASP ASN ALA THR ILE ARG VAL THR ASN LEU SER GLU ASP
SEQRES 3 A 103 THR ARG GLU THR ASP LEU GLN GLU LEU PHE ARG PRO PHE
SEQRES 4 A 103 GLY SER ILE SER ARG ILE TYR LEU ALA LYS ASP LYS THR
SEQRES 5 A 103 THR GLY GLN SER LYS GLY PHE ALA PHE ILE SER PHE HIS
SEQRES 6 A 103 ARG ARG GLU ASP ALA ALA ARG ALA ILE ALA GLY VAL SER
SEQRES 7 A 103 GLY PHE GLY TYR ASP HIS LEU ILE LEU ASN VAL GLU TRP
SEQRES 8 A 103 ALA LYS PRO SER THR ASN SER GLY PRO SER SER GLY
HELIX 1 1 ARG A 251 GLU A 257 1 7
HELIX 2 2 ARG A 289 VAL A 300 1 12
SHEET 1 A 4 ILE A 265 LYS A 272 0
SHEET 2 A 4 SER A 279 PHE A 287 -1 O SER A 286 N ARG A 267
SHEET 3 A 4 ALA A 239 THR A 244 -1 N VAL A 243 O ALA A 283
SHEET 4 A 4 ASN A 311 TRP A 314 -1 O GLU A 313 N ARG A 242
SHEET 1 B 2 GLY A 304 TYR A 305 0
SHEET 2 B 2 LEU A 308 ILE A 309 -1 O LEU A 308 N TYR A 305
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 9 2 Bytes